ID A0A1F1ZX06_9CORY Unreviewed; 1705 AA.
AC A0A1F1ZX06;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OFT91770.1};
GN ORFNames=HMPREF3098_00240 {ECO:0000313|EMBL:OFT91770.1};
OS Corynebacterium sp. HMSC28B08.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581066 {ECO:0000313|EMBL:OFT91770.1, ECO:0000313|Proteomes:UP000177449};
RN [1] {ECO:0000313|EMBL:OFT91770.1, ECO:0000313|Proteomes:UP000177449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC28B08 {ECO:0000313|EMBL:OFT91770.1,
RC ECO:0000313|Proteomes:UP000177449};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFT91770.1}.
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DR EMBL; LWOT01000004; OFT91770.1; -; Genomic_DNA.
DR RefSeq; WP_070433546.1; NZ_KV786132.1.
DR STRING; 1581066.HMPREF3098_00240; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000177449; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; NF040607; mycolic_Pks13; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..94
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 119..542
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1195..1269
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1126..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1705 AA; 180198 MW; 8A691953AF1B68B2 CRC64;
MEDNLTVGSA SSNNRPTSIS EMRQWLRDWV AKTTGLSPQQ ITDDRSMEEF GLSSRDVVIL
SGDLERLTGQ NLDATVAYEF NSIAALADYL INGRGSISSD AAFFPAQGGA SGQALSPDDR
DVAIVGVAGR YPGANSADEM WEMFLGYRSG VGELPAGRWS EYAGDKEMTR RMEEAVLTGG
YLEDIAAFDA EFFGLSPVEA ANMDPQQRIV LQLTWEALEN AGIPANQLRG LPVGVFMASN
NNDYGMLISA DPTEAHPYAL TGNSSAIIAN RISYAFDFRG PSISVDTACS ASLVSIHQAV
RSLRDGDSTV AIAGGVNILS NPFGTVAFSE LGVLSPTGKI HAFSDDADGI VRSDGAGVVV
LKRLSDARRD GDKVLAVIKG SAVNSDGRSN GLTAPNPDAQ VDVLRAAYRD AGISPTHVDY
VEAHGTGTIL GDPIEATALG AVLSGPRDAA NPLLLGSAKT NFGHTEAAAG VAGVIKVVKA
MEHGTIPPSL NYAGPNPYID FDGAHLEVVE DAREWPAYSG RPVAGVSGFG FGGTNAHVVI
TAPEAQQPEL ADDVTPAGGA LVADEGVEQK YILPVSGLLP SRRRHAAEDL ATWLEENRDS
KGVTLESVAR ALAGRNHGRS RGAILAGDFD QAIDGLRRLA DKRSGAHVKS ADSPSTTGPV
WVYSGFGSQH RKMGKELYEM SPFFAARLRE LDEVVQRESG WSLVEKILDD DQDFDTESAQ
VGITCIQIAL TELLQHLGVK PSAVVGQSMG EIAAAFAVGG LSKEDAVLVA CHRSRLMGEG
EQNLPEDKQG AMAVVEFGVE ELATFTSEHP EFAKVEPAVY AAPGMTTVGG PREPVAKLVE
HLESEGKFAR LLPVKGAGHT SMLDPILGEL HFEIGDIQPR PIHTPLYSTV DRGRVYRPGE
TLHDADYFVR CTRQPVWFRD ATGQQFDDGF RTFVEISPNP VALMPLMNNS FAHDASDSKL
LYLLKRKEPA GETVANCLAE LYVQGSGVDL KALVGPFGAT ATVPGVRWNL QRHWTNARPA
SGGVAGLPGV RVDLPDGRVA FSVGADLVPS VLALAEAVAE QVAPGAQVVA SEEHAVLPSA
GSLTAMATKS LGGWSVEVYD AETSSAMPLV GEAFVSTLAV AAPGGSLSDA KASPAGGSLD
ATNSPAGEKP GVGSGAIAGA ATGATGGRAT GAGTKNHALP EVDTDAMRWS PESGESVADR
LRSIVGESMG YDVEDLPGEL PLIDLGLDSL MGMRIKNRVE YDFDLPPLQV QTLRDGSVDD
VITMVERMVA EKGANPATDS TGADDAATGD QKGTATGGQK DTAAGDQKDT AGSVKTSDYT
AAAGGVAPRD ASERLVFATW AKVTGKAAPG VTSPLPEISD EKAAELAERL SDRSGGEITA
QDVQNADSME PLADLVRAKL ETAVEGNIRV LRAREDGAAG SGAEGANSGE DSDAPRKPSV
FLFHPAGGSS VVFQPLMRRL PADIPVYGVE RLEGELSDRA AQYLDEIIEY SAGMPVVLGG
WSFGGALAYE VANQFAQRAE RGEPTVEISR IVLLDTVQPK NPAPDTKEEM HKRWDRYAEF
ARRTYGLPLE VPHDLLDEHG EGVMLTMFQQ FLTSPEVGGL GLPAGVLEHQ RASFVDNRIL
ESLDFSQWAT VSAPVTLFRA ERMHDGAIEL EPAYAEVAED GGWAQIVDDL KIVHLNGDHL
AIVDEPEIGK VGKVLAQQIE EDLKR
//
